Calcium in PDB 1fo4: Crystal Structure of Xanthine Dehydrogenase Isolated From Bovine Milk

All present enzymatic activity of Crystal Structure of Xanthine Dehydrogenase Isolated From Bovine Milk:
1.1.1.204;

The structure of Crystal Structure of Xanthine Dehydrogenase Isolated From Bovine Milk, PDB code: 1fo4 was solved by C.Enroth, B.T.Eger, K.Okamoto, T.Nishino, T.Nishino, E.F.Pai, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 2.10
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	169.451, 124.493, 148.327, 90.00, 90.94, 90.00
R / Rfree (%)	19.8 / 23.8

The structure of Crystal Structure of Xanthine Dehydrogenase Isolated From Bovine Milk also contains other interesting chemical elements:

Molybdenum	(Mo)	2 atoms
Iron	(Fe)	8 atoms

The binding sites of Calcium atom in the Crystal Structure of Xanthine Dehydrogenase Isolated From Bovine Milk (pdb code 1fo4). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Xanthine Dehydrogenase Isolated From Bovine Milk, PDB code: 1fo4:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Xanthine Dehydrogenase Isolated From Bovine Milk


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Xanthine Dehydrogenase Isolated From Bovine Milk within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca4009 b:21.7 occ:1.00 OG A:SER874 2.6 23.0 1.0 OG A:SER907 2.6 20.8 1.0 O A:SER870 2.7 20.6 1.0 O A:ALA867 2.7 23.1 1.0 O A:ASN908 2.7 20.5 1.0 O A:ARG871 3.0 22.8 1.0 C A:ARG871 3.5 22.1 1.0 N A:ASN908 3.5 20.9 1.0 C A:ALA867 3.7 22.7 1.0 C A:SER870 3.7 21.2 1.0 CB A:ASP872 3.7 21.6 1.0 C A:ASN908 3.8 21.1 1.0 CB A:SER907 3.8 20.4 1.0 CB A:SER874 3.9 23.0 1.0 NE2 A:HIS840 3.9 19.8 1.0 CB A:ALA867 3.9 22.9 1.0 C A:SER907 4.0 21.3 1.0 CA A:SER907 4.1 21.1 1.0 CA A:ALA867 4.1 22.9 1.0 CA A:ARG871 4.1 22.4 1.0 N A:ASP872 4.2 21.8 1.0 CA A:ASN908 4.2 21.0 1.0 N A:ARG871 4.3 21.5 1.0 CA A:ASP872 4.5 22.0 1.0 CE1 A:HIS840 4.5 20.6 1.0 N A:SER874 4.5 22.1 1.0 OG A:SER870 4.5 21.3 1.0 CA A:SER874 4.7 22.7 1.0 N A:GLY868 4.8 22.9 1.0 CA A:SER870 4.8 21.1 1.0 N A:SER870 4.8 22.0 1.0 CB A:ASN908 4.8 20.6 1.0 N A:LEU873 4.8 22.1 1.0 CG A:ASP872 4.9 21.8 1.0 C A:ASP872 4.9 22.0 1.0 N A:THR909 4.9 20.9 1.0 O A:SER907 5.0 22.0 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Xanthine Dehydrogenase Isolated From Bovine Milk


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Xanthine Dehydrogenase Isolated From Bovine Milk within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca4019 b:24.4 occ:1.00 OG B:SER874 2.6 22.3 1.0 OG B:SER907 2.7 22.8 1.0 O B:SER870 2.7 22.4 1.0 O B:ALA867 2.7 19.1 1.0 O B:ASN908 2.8 23.2 1.0 O B:ARG871 3.0 22.6 1.0 C B:ARG871 3.5 22.8 1.0 N B:ASN908 3.5 23.3 1.0 CB B:ASP872 3.7 22.6 1.0 C B:ALA867 3.7 20.8 1.0 C B:SER870 3.7 23.0 1.0 C B:ASN908 3.8 23.3 1.0 CB B:SER907 4.0 22.4 1.0 NE2 B:HIS840 4.0 21.3 1.0 CB B:SER874 4.0 22.9 1.0 C B:SER907 4.1 23.8 1.0 CB B:ALA867 4.1 22.4 1.0 N B:ASP872 4.1 22.7 1.0 CA B:ARG871 4.2 23.6 1.0 CA B:SER907 4.2 23.0 1.0 CA B:ASN908 4.2 22.9 1.0 CA B:ALA867 4.2 21.5 1.0 N B:ARG871 4.4 23.0 1.0 CA B:ASP872 4.4 22.9 1.0 CE1 B:HIS840 4.5 21.7 1.0 OG B:SER870 4.5 24.4 1.0 N B:SER874 4.5 22.8 1.0 CB B:ASN908 4.7 22.7 1.0 CG B:ASP872 4.8 23.1 1.0 N B:LEU873 4.8 22.9 1.0 N B:SER870 4.8 22.3 1.0 CA B:SER874 4.8 23.3 1.0 CA B:SER870 4.8 22.5 1.0 C B:ASP872 4.8 22.8 1.0 N B:GLY868 4.9 20.5 1.0 OD1 B:ASP872 4.9 22.6 1.0 N B:THR909 5.0 21.9 1.0 O B:SER907 5.0 24.6 1.0

C.Enroth, B.T.Eger, K.Okamoto, T.Nishino, T.Nishino, E.F.Pai. Crystal Structures of Bovine Milk Xanthine Dehydrogenase and Xanthine Oxidase: Structure-Based Mechanism of Conversion. Proc.Natl.Acad.Sci.Usa V. 97 10723 2000.
ISSN: ISSN 0027-8424
PubMed: 11005854
DOI: 10.1073/PNAS.97.20.10723